ArticleThe Journal of biological chemistry2015
Topological analysis of Hedgehog acyltransferase, a multipalmitoylated transmembrane protein.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
41 citing papers in PubMed, 60 citations in OpenAlex.
- Palmitoylation in cancer: decoding its roles in signal transduction, tumor immunity, and emerging therapeutic opportunities.Frontiers in immunology · 2025Review
- Protein lipidation in cancer: mechanisms, dysregulation and emerging drug targets.Nature reviews. Cancer · 2024Review
- Design, Synthesis, and Evaluation of Inhibitors of Hedgehog Acyltransferase.Journal of medicinal chemistry · 2024Article
- Therapeutic potential of ghrelin/GOAT/GHSR system in gastrointestinal disorders.Frontiers in nutrition · 2024Review
- Review
- A rising tide lifts all MBOATs: recent progress in structural and functional understanding of membrane boundFrontiers in physiology · 2023Review
- Structure, mechanism, and inhibition of Hedgehog acyltransferase.Molecular cell · 2021Article
- Hedgehog acyl-transferase-related multiple congenital anomalies: Report of an additional family and delineation of the syndrome.American journal of medical genetics. Part A · 2021Article
- Ghrelin octanoylation by ghrelinOpen biology · 2021Review
- A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications.Chemical reviews · 2021Review
- Photochemical Probe Identification of a Small-Molecule Inhibitor Binding Site in Hedgehog Acyltransferase (HHAT).Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- Photochemical Probe Identification of a Small-Molecule Inhibitor Binding Site in Hedgehog Acyltransferase (HHAT)*.Angewandte Chemie (International ed. in English) · 2021Article
- Determination of the membrane topology of PORCN, an O-acyl transferase that modifies Wnt signalling proteins.Open biology · 2021Article
- Palmitoylation of Hedgehog proteins by Hedgehog acyltransferase: roles in signalling and disease.Open biology · 2021Review
- An overview of ghrelinExpert opinion on therapeutic patents · 2020Review
- Ghrelin Signaling: GOAT and GHS-R1a Take a LEAP in Complexity.Trends in endocrinology and metabolism: TEM · 2020Review
- Metabonomic-Transcriptome Integration Analysis on Osteoarthritis and Rheumatoid Arthritis.International journal of genomics · 2020Article
- C-Terminal Peptide Modifications Reveal Direct and Indirect Roles of Hedgehog Morphogen Cholesteroylation.Frontiers in cell and developmental biology · 2020Article
- Hedgehog Acyltransferase Promotes Uptake of Palmitoyl-CoA across the Endoplasmic Reticulum Membrane.Cell reports · 2019Article
- Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Hedgehog proteins are secreted morphogens that play critical roles in development and disease. During maturation of the proteins through the secretory pathway, they are modified by the addition of N-terminal palmitic acid and C-terminal cholesterol moieties, both of which are critical for their correct function and localization. Hedgehog acyltransferase (HHAT) is the enzyme in the endoplasmic reticulum that palmitoylates Hedgehog proteins, is a member of a small subfamily of membrane-bound O-acyltransferase proteins that acylate secreted proteins, and is an important drug target in cancer. However, little is known about HHAT structure and mode of function. We show that HHAT is comprised of ten transmembrane domains and two reentrant loops with the critical His and Asp residues on opposite sides of the endoplasmic reticulum membrane. We further show that HHAT is palmitoylated on multiple cytosolic cysteines that maintain protein structure within the membrane. Finally, we provide evidence that mutation of the conserved His residue in the hypothesized catalytic domain results in a complete loss of HHAT palmitoylation, providing novel insights into how the protein may function in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.